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Characterization of sgce6, the flavin reductase component supporting fad-dependent halogenation and hydroxylation in the biosynthesis of the enediyne antitumor antibiotic c-1027

Academic Article
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Overview

authors

  • Van Lanen, S. G.
  • Lin, S. J.
  • Horsman, G. P.
  • Shen, Ben

publication date

  • November 2009

journal

  • FEMS Microbiology Letters  Journal

abstract

  • The C-1027 enediyne antitumor antibiotic from Streptomyces globisporus possesses an (S)-3-chloro-5-hydroxy-beta-tyrosine moiety, the chloro- and hydroxy-substituents of which are installed by a flavin-dependent halogenase SgcC3 and monooxygenase SgcC, respectively. Interestingly, a single flavin reductase, SgcE6, can provide reduced flavin to both enzymes. Bioinformatics analysis reveals that, similar to other flavin reductases involved in natural product biosynthesis, SgcE6 belongs to the HpaC-like subfamily of the Class I flavin reductases. The present study describes the steady-state kinetic characterization of SgcE6 as a strictly NADH- and FAD-specific enzyme.

subject areas

  • Amino Acid Sequence
  • Aminoglycosides
  • Antineoplastic Agents
  • Bacterial Proteins
  • Biosynthetic Pathways
  • Cluster Analysis
  • Enediynes
  • Flavin-Adenine Dinucleotide
  • Halogenation
  • Hydroxylation
  • Kinetics
  • Molecular Sequence Data
  • NAD
  • Oxidoreductases
  • Phylogeny
  • Sequence Homology
  • Streptomyces
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Research

keywords

  • C-1027
  • SgcE6
  • enediyne
  • flavin reductase
  • halogenase
  • monooxygenase
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Identity

PubMed Central ID

  • PMC2767520

International Standard Serial Number (ISSN)

  • 0378-1097

Digital Object Identifier (DOI)

  • 10.1111/j.1574-6968.2009.01802.x

PubMed ID

  • 19817865
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Additional Document Info

start page

  • 237

end page

  • 241

volume

  • 300

issue

  • 2

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